Publications

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Simmons, H. C., Watanabe, A., Iii, T. H. Oguin, Van Itallie, E. S., Wiehe, K. J., Sempowski, G. D., Kuraoka, M., Kelsoe, G., and McCarthy, K. R. (2023) A new class of antibodies that overcomes a steric barrier to cross-group neutralization of influenza viruses. PLoS Biol. 21, e3002415
Simon, B., Lou, H. Jane, Huet-Calderwood, C., Shi, G., Boggon, T. J., Turk, B. E., and Calderwood, D. A. (2022) Tousled-like kinase 2 targets ASF1 histone chaperones through client mimicry. Nat Commun. 13, 749
Simonovic, M., and Steitz, T. A. (2008) Peptidyl-CCA deacylation on the ribosome promoted by induced fit and the O3'-hydroxyl group of A76 of the unacylated A-site tRNA. RNA. 14, 2372-8
Simpson, B. W., Pahil, K. S., Owens, T. W., Lundstedt, E. A., Davis, R. M., Kahne, D., and Ruiz, N. (2019) Combining Mutations That Inhibit Two Distinct Steps of the ATP Hydrolysis Cycle Restores Wild-Type Function in the Lipopolysaccharide Transporter and Shows that ATP Binding Triggers Transport. MBio. 10.1128/mBio.01931-19
Sinatra, L., Vogelmann, A., Friedrich, F., Tararina, M. A., Neuwirt, E., Colcerasa, A., König, P., Toy, L., Yesiloglu, T. Z., Hilscher, S., Gaitzsch, L., Papenkordt, N., Zhai, S., Zhang, L., Romier, C., Einsle, O., Sippl, W., Schutkowski, M., Gross, O., Bendas, G., Christianson, D. W., Hansen, F. K., Jung, M., and Schiedel, M. (2023) Development of First-in-Class Dual Sirt2/HDAC6 Inhibitors as Molecular Tools for Dual Inhibition of Tubulin Deacetylation. J Med Chem. 66, 14787-14814
Singer, J. M., Novotney, S., Strickland, D., Haddox, H. K., Leiby, N., Rocklin, G. J., Chow, C. M., Roy, A., Bera, A. K., Motta, F. C., Cao, L., Strauch, E. - M., Chidyausiku, T. M., Ford, A., Ho, E., Zaitzeff, A., Mackenzie, C. O., Eramian, H., DiMaio, F., Grigoryan, G., Vaughn, M., Stewart, L. J., Baker, D., and Klavins, E. (2022) Large-scale design and refinement of stable proteins using sequence-only models. PLoS One. 17, e0265020
Singh, H., Reilly, T. J., and Tanner, J. J. (2011) Structural basis of the inhibition of class C acid phosphatases by adenosine 5'-phosphorothioate. FEBS J. 278, 4374-81
Singh, M., Wang, Z., Koo, B. - K., Patel, A., Cascio, D., Collins, K., and Feigon, J. (2012) Structural basis for telomerase RNA recognition and RNP assembly by the holoenzyme La family protein p65. Mol Cell. 47, 16-26
Singh, M., Gonzales, F. A., Cascio, D., Heckmann, N., Chanfreau, G., and Feigon, J. (2009) Structure and functional studies of the CS domain of the essential H/ACA ribonucleoparticle assembly protein SHQ1. J Biol Chem. 284, 1906-16
Singh, M., Wang, Z., Cascio, D., and Feigon, J. (2015) Structure and interactions of the CS domain of human H/ACA RNP assembly protein Shq1. J Mol Biol. 427, 807-23
Singh, H., Felts, R. L., Schuermann, J. P., Reilly, T. J., and Tanner, J. J. (2009) Crystal Structures of the histidine acid phosphatase from Francisella tularensis provide insight into substrate recognition. J Mol Biol. 394, 893-904
Singh, H., Arentson, B. W., Becker, D. F., and Tanner, J. J. (2014) Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site. Proc Natl Acad Sci U S A. 111, 3389-94
Singh, S., Ng, J., Nayak, D., and Sivaraman, J. (2019) Structural insights into a HECT-type E3 ligase AREL1 and its ubiquitination activities . J Biol Chem. 294, 19934-19949
Singh, S., and Sivaraman, J. (2020) Crystal structure of HECT domain of UBE3C E3 ligase and its ubiquitination activity. Biochem J. 477, 905-923
Singh, H., Schuermann, J. P., Reilly, T. J., Calcutt, M. J., and Tanner, J. J. (2010) Recognition of nucleoside monophosphate substrates by Haemophilus influenzae class C acid phosphatase. J Mol Biol. 404, 639-49
Singh, A. K., Saotome, K., and Sobolevsky, A. I. (2017) Swapping of transmembrane domains in the epithelial calcium channel TRPV6. Sci Rep. 7, 10669
Singh, A. K., Saotome, K., McGoldrick, L. L., and Sobolevsky, A. I. (2018) Structural bases of TRP channel TRPV6 allosteric modulation by 2-APB. Nat Commun. 9, 2465
Singla, N., Goldgur, Y., Xu, K., Paavilainen, S., Nikolov, D. B., and Himanen, J. P. (2010) Crystal structure of the ligand-binding domain of the promiscuous EphA4 receptor reveals two distinct conformations. Biochem Biophys Res Commun. 399, 555-9
Sinha, S., Cheng, S., Sung, Y. Won, McNamara, D. E., Sawaya, M. R., Yeates, T. O., and Bobik, T. A. (2014) Alanine scanning mutagenesis identifies an asparagine-arginine-lysine triad essential to assembly of the shell of the Pdu microcompartment. J Mol Biol. 426, 2328-45
Sit, B., Crowley, S. M., Bhullar, K., Lai, C. Chieh- Lin, Tang, C., Hooda, Y., Calmettes, C., Khambati, H., Ma, C., Brumell, J. H., Schryvers, A. B., Vallance, B. A., and Moraes, T. F. (2015) Active Transport of Phosphorylated Carbohydrates Promotes Intestinal Colonization and Transmission of a Bacterial Pathogen. PLoS Pathog. 11, e1005107
Siu, K. K., Sultana, A., Azimi, F. C., and Lee, J. E. (2013) Structural determinants of HIV-1 Vif susceptibility and DNA binding in APOBEC3F. Nat Commun. 4, 2593
Sivakumaren, S. Carmen, Shim, H., Zhang, T., Ferguson, F. M., Lundquist, M. R., Browne, C. M., Seo, H. - S., Paddock, M. N., Manz, T. D., Jiang, B., Hao, M. - F., Krishnan, P., Wang, D. G., T Yang, J., Kwiatkowski, N. P., Ficarro, S. B., Cunningham, J. M., Marto, J. A., Dhe-Paganon, S., Cantley, L. C., and Gray, N. S. (2020) Targeting the PI5P4K Lipid Kinase Family in Cancer Using Covalent Inhibitors. Cell Chem Biol. 10.1016/j.chembiol.2020.02.003
Sjekloća, L., and Ferré-D'Amaré, A. R. (2019) Binding between G Quadruplexes at the Homodimer Interface of the Corn RNA Aptamer Strongly Activates Thioflavin T Fluorescence. Cell Chem Biol. 26, 1159-1168.e4
Slater, B. T., Han, X., Chen, L., and Xiong, Y. (2020) Structural insight into T cell coinhibition by PD-1H (VISTA). Proc Natl Acad Sci U S A. 10.1073/pnas.1908711117
Slavik, K. M., Morehouse, B. R., Ragucci, A. E., Zhou, W., Ai, X., Chen, Y., Li, L., Wei, Z., Bähre, H., König, M., Seifert, R., S Y Lee, A., Cai, H., Imler, J. - L., and Kranzusch, P. J. (2021) cGAS-like receptors sense RNA and control 3'2'-cGAMP signaling in Drosophila. Nature. 10.1038/s41586-021-03743-5

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